4.1.1.9: malonyl-CoA decarboxylase
This is an abbreviated version!
For detailed information about malonyl-CoA decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.9
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4.1.1.9
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carnitine
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malonic
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amp-activated
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palmitoyltransferase
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aciduria
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goose
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uropygial
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methylmalonyl-coa
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methylmalonic
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medicine
- 4.1.1.9
- carnitine
-
malonic
-
amp-activated
- palmitoyltransferase
-
aciduria
- goose
-
uropygial
- methylmalonyl-coa
-
methylmalonic
- medicine
Reaction
Synonyms
Acyl-CoA: malonate CoA transferase/malonyl-CoA decarboxylase, Decarboxylase, malonyl coenzyme A, hMCD, malonyl CoA decarboxylase, Malonyl coenzyme A decarboxylase, Malonyl-CoA decarboxylase, malonyl-CoA decarboxylase/acetyltransferase, malonyl-coenzyme A decarboxylase, MCD, MLYCD
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General Information
General Information on EC 4.1.1.9 - malonyl-CoA decarboxylase
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evolution
malfunction
physiological function
additional information
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the MCD catalytic domain is structurally homologous to those of the GCN5-related N-acetyltransferase superfamily, especially the curacin A polyketide synthase catalytic module, with a conserved His-Ser/Thr dyad important for catalysis
evolution
the MCD catalytic domain is structurally homologous to those of the GCN5-related N-acetyltransferase superfamily, especially the curacin A polyketide synthase catalytic module, with a conserved His-Ser/Thr dyad important for catalysis
evolution
the MCD catalytic domain is structurally homologous to those of the GCN5-related N-acetyltransferase superfamily, especially the curacin A polyketide synthase catalytic module, with a conserved His-Ser/Thr dyad important for catalysis
evolution
the MCD catalytic domain is structurally homologous to those of the GCN5-related N-acetyltransferase superfamily, especially the curacin A polyketide synthase catalytic module, with a conserved His-Ser/Thr dyad important for catalysis
evolution
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the MCD catalytic domain is structurally homologous to those of the GCN5-related N-acetyltransferase superfamily, especially the curacin A polyketide synthase catalytic module, with a conserved His-Ser/Thr dyad important for catalysis
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impact of loss-of-function alleles in hereditary MCD deficiency
malfunction
MLYCD deficiency, OMIM 248360, also known as malonic aciduria, is a rare autosomal recessively inherited inborn error of fatty acid metabolism. A patient with this enzyme deficiency shows signs of neonatal hypoglycemia, mental retardation, developmental delay and rheumatoid arthritis. The brain shows patchy, symmetrical hyperintensity of the deep white matter with periventricular white matter and subcortical arcuate fibers being spared. Protein mislocalization to the nucleus is a characteristic feature of MLYCD deficiency in the patient. Phenotype, overview. The phenotype probably involves mutations H152N and M1K
malfunction
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pharmacological inhibition of malonyl-CoA decarboxylase reduces the inflammatory response associated with insulin resistance. Additionally, inhibition of MCD strongly diminishes lipopolysaccharide-induced activation of palmitate oxidation and prevents lipopolysaccharide-induced collapse of total cellular antioxidant capacity and prevents increases in the level of ceramide in cardiomyocytes and macrophages while also ameliorating LPS-initiated decreases in PPAR binding. Genetic inactivation of malonyl-CoA decarboxylase protects mice against high-fat diet-induced insulin resistance
malfunction
decreased fat oxidation in enzyme-deficient mice results in the accumulation of lipid intermediates in peripheral tissues, but this is not associated with a worsening of age-associated insulin resistance and, conversely, improves longevity. This improvement is associated with reduced oxidative stress and reduced acetylation of the antioxidant enzyme superoxide dismutase 2 in muscle but not the liver
malfunction
enzyme inhibition by an ultrasound-mediated injection of miRNA into the rat myocardium increases energy reserves in the left ventricle after myocardial infarction
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malonyl-CoA is both a substrate for fatty acid synthase and an inhibitor of fatty acid oxidation acting as a metabolic switch between anabolic fatty acid synthesis and catabolic fatty acid oxidation
physiological function
decarboxylation of malonyl-CoA to acetyl-CoA by malonyl-CoA decarboxylase is an essential facet in the regulation of fatty acid metabolism
physiological function
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malonyl-CoA decarboxylase regulates fatty acid oxidation
physiological function
the enzyme provides a route for disposal of malonyl-CoA from mitochondria and peroxisomes, whereas in the cytosol the malonyl-CoA pool is regulated by the balance of th enzyme and acetyl-CoA carboxylase activities
physiological function
a two week induction of the enzyme in skeletal muscle does not alter body weight or ameliorate glucose intolerance, conversely it further impairs insulin signaling in the skeletal muscle of diet-induced obese mice. Furthermore, an acute induction of the enzyme leads to a suppression of fatty acid oxidative genes suggesting a redundant and metabolite driven regulation of gene expression
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catalytic domain structure and active site structure comparisons, overview
additional information
catalytic domain structure and active site structure comparisons, overview
additional information
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catalytic domain structure and active site structure comparisons, overview
additional information
catalytic domain structure and active site structure comparisons, overview
additional information
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catalytic domain structure and active site structure comparisons, overview
additional information
catalytic domain structure and active site structure, with His-Ser/Thr dyad, comparisons, overview. The catalytic domain of MCD contains a central eight-stranded, mostly antiparallel etab sheet (beta1-beta8) that is surrounded by at least 11 alpha helices. The substrate can position its thioester carbonyl, bridging the carboxylate leaving group and CoA backbone, in the vicinity of Ser329 and His423
additional information
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catalytic domain structure and active site structure, with His-Ser/Thr dyad, comparisons, overview. The catalytic domain of MCD contains a central eight-stranded, mostly antiparallel etab sheet (beta1-beta8) that is surrounded by at least 11 alpha helices. The substrate can position its thioester carbonyl, bridging the carboxylate leaving group and CoA backbone, in the vicinity of Ser329 and His423
additional information
structural asymmetry and disulfide bridges among subunits modulate the activity of the enzyme. The molecular organization of dimer of structural heterodimers, in which the two subunits present markedly different conformations, is consistent with half-of-the-sites reactivity. Interactions extend beyond the C-terminal targeting motif. Active site structure, overview
additional information
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structural asymmetry and disulfide bridges among subunits modulate the activity of the enzyme. The molecular organization of dimer of structural heterodimers, in which the two subunits present markedly different conformations, is consistent with half-of-the-sites reactivity. Interactions extend beyond the C-terminal targeting motif. Active site structure, overview
additional information
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catalytic domain structure and active site structure comparisons, overview
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